Ionizing Radiation-Induced Crosslinking in Proteins

Yamamoto, Osamu

doi:10.1007/978-1-4684-3282-4_31

Cited by 20 publications

(3 citation statements)

References 145 publications

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“…Further possible reactions of sulfhydryl groups upon X-irradiation might be e.g., the oxidation to sulfoxides, which might give rise to non-covalent cross-linking, or the formation of covalent disulfide bridges (cf. Yamamoto, 1977).…”

Section: Nature Of Radiation Damagesmentioning

confidence: 95%

“…Yamamoto, 1977;Grossweiner, 1976). Malate synthase contains cys, met and a lot of the aromatic amino acids; obviously one cys per subunit is situated on the enzyme surface because it is reactive towards Ellman's reagent in the native state; cys and trp were found to be correlated with substrate binding and/or enzymic activity (Schmid et al, 1974;Durchschlag et al, 1977Durchschlag et al, , 1978.…”

Section: Nature Of Radiation Damagesmentioning

confidence: 96%

“…The effects of ionizing radiation on various proteins in aqueous solutions have been described previously (e.g., Dertinger and Jung, 1969;Schiigler, 1973;Yamamoto, 1977;Lynn, 1977;Armstrong and Buchanan, 1978). Radiation induced damages involve chain cleavage, changes in amino acid composition, destruction of secondary and tertiary structure, aggregation phenomena etc.…”

Section: Introductionmentioning

confidence: 96%

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Small-angle X-ray scattering studies on the X-ray induced aggregation of malate synthase

Zipper

Durchschlag

1980

Radiat Environ Biophys

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Summary.Malate synthase was investigated by the small-angle X-ray scattering technique in aqueous solution. Measurements extending for several hours revealed a continuous increase of the intensity in the innermost portion of the scattering curve. There is clear evidence that this increase was caused by an X-ray induced aggregation of enzyme particles during the performance of the small-angle X-ray scattering experiment. The monitoring of the aggregation process in situ by means of small-angle X-ray scattering led to a model of the way how the aggregation might proceed. The analysis of the scattering curves of malate synthase taken at various stages of aggregation established the retention of the thickness factor of the native enzyme and the occurrence of one and later on of two cross-section factors. The process of aggregation was also reflected by the increase of extension of the distance distribution function. According to these results, th~ first step of aggregation might be a linear side-by-side association of the oblate enzyme particles, a process which is followed by a twodimensional aggregation. An aggregation in the third dimension was not observed during the time covered by our experiment. The predominance of aggregation in only one or two dimensions was corroborated by comparison of appropriate theoretical scattering curves with the experimental curves. The theoretical scattering curves for this comparison were obtained by averaging over the properly weighted scattering curves calculated for various species of hypothetical aggregates. The time dependence of the apparent mean radius of gyration was used to compare the aggregation of enzyme samples that were irradiated under different experimental conditions. It turned out that by addition of dithiothreitol to the enzyme solutions as well as in the presence of the substrates (acetyl-CoA, glyoxylate) or of a substrate analogue (pyruvate) or of ethanol the rate of aggregation is reduced. Enzymic activity was found to decrease about exponentially with increasing X-ray dose. The presence of dithiothreitol or of the substrate glyoxylate or of the substrate analogue pyruvate protects the enzyme against X-ray induced inactivation. The substrate acetyl-CoA does not exhibit a comparable protective effect against 0301-634X/80/0018/0099/$ 04.60 100 P. Zipper and H. Durchschlag inactivation. Measurements of enzymic activity and small-angle X-ray scattering on samples, which had been X-irradiated with a defined dose prior to the measurements, established two different series of efficiency for the protection of the enzyme against aggregation (pyruvate > glyoxylate > acetyl-CoA) and inactivation (glyoxylate > pyruvate ,> acetyl-CoA). The results showed that there is no direct relation between the extent of aggregation and the loss of enzymic activity.

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Section: Nature Of Radiation Damagesmentioning

confidence: 95%

Section: Nature Of Radiation Damagesmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 96%

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Small-angle X-ray scattering studies on the X-ray induced aggregation of malate synthase

Zipper

Durchschlag

1980

Radiat Environ Biophys

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Investigation of radical‐based damage of RNase A in aqueous solution and lipid vesicles

Torreggiani¹,

Tamba²,

Manco

et al. 2005

Biopolymers

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The gamma-irradiation of bovine pancreatic ribonuclease A (RNase A) in aqueous solution were investigated at different doses by vibrational spectroscopy as well as enzymatic assay, electrophoresis, and HPLC analysis. Both functional and structural changes of the protein were caused by attack of H(*) atoms and (*)OH radicals. In particular, Raman spectroscopy was shown to be a useful tool in identifying conformational changes of the protein structure and amino acidic residues that are preferential sites of the radical attack (i.e., tyrosine and methionine). After partial structural changes by the initial radical attack, the internal sulfur-containing amino acid residues were rendered susceptible to transformation. By using the biomimetic model of dioleoyl phosphatidyl choline vesicle suspensions containing RNase A, the damage to methione residues could be connected to a parallel alteration of membrane unsaturated lipids. In fact, thiyl radical species formed from protein degradation can diffuse into the lipid bilayer and cause isomerization of the naturally occurring cis double bonds. As a consequence, trans unsaturated fatty acids are formed in vesicles and can be considered to be markers of this protein damage.

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Radiation-induced changes of structural and functional properties of human hemoglobin

Szweda‐Lewandowska

Puchała

Osmulski

et al. 1989

Radiat Environ Biophys

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Gel filtration and SDS-PAGE separation of hemoglobin (Hb) irradiated under argon or N2O show formation of covalent-aggregated Hb molecules. The production of covalent bonds is attributed mainly to the action of hydroxyl radicals, because addition of ethanol, a scavenger of these radicals, suppresses this reaction to a great extent. The oxidized heme iron forming metHb or hemichromes is found in all the separated fractions of irradiated Hb. It is also found that the radiation-modified Hb molecules exhibit a decrease of co-operative binding of oxygen.

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Ionizing Radiation-Induced Crosslinking in Proteins

Cited by 20 publications

References 145 publications

Small-angle X-ray scattering studies on the X-ray induced aggregation of malate synthase

Small-angle X-ray scattering studies on the X-ray induced aggregation of malate synthase

Investigation of radical‐based damage of RNase A in aqueous solution and lipid vesicles

Radiation-induced changes of structural and functional properties of human hemoglobin

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